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Protein

Protein Shroom2

Gene

Shroom2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Shroom2
Alternative name(s):
Liver regeneration-related protein LRRG167
Protein Apxl
Gene namesi
Name:Shroom2
Synonyms:Apxl
ORF Names:Ab2-404
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi1565163. Shroom2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14231423Protein Shroom2PRO_0000286064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031PhosphoserineCombined sources
Modified residuei185 – 1851PhosphoserineCombined sources
Modified residuei197 – 1971PhosphoserineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei806 – 8061PhosphoserineBy similarity
Modified residuei830 – 8301PhosphoserineBy similarity
Modified residuei831 – 8311PhosphoserineCombined sources
Modified residuei833 – 8331PhosphoserineBy similarity
Modified residuei834 – 8341PhosphothreonineBy similarity
Modified residuei918 – 9181PhosphoserineCombined sources
Modified residuei920 – 9201PhosphoserineCombined sources
Modified residuei1072 – 10721PhosphoserineBy similarity
Modified residuei1329 – 13291PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ7TP36.
PRIDEiQ7TP36.

PTM databases

iPTMnetiQ7TP36.
PhosphoSiteiQ7TP36.

Expressioni

Gene expression databases

ExpressionAtlasiQ7TP36. baseline and differential.

Interactioni

Subunit structurei

Interacts with F-actin.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000056187.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini575 – 677103ASD1PROSITE-ProRule annotationAdd
BLAST
Domaini1092 – 1418327ASD2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 9087Ser-richAdd
BLAST

Domaini

The ASD1 domain mediates F-actin binding.By similarity

Sequence similaritiesi

Belongs to the shroom family.Curated
Contains 1 ASD1 domain.PROSITE-ProRule annotation
Contains 1 ASD2 domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.Curated

Phylogenomic databases

eggNOGiENOG410II86. Eukaryota.
ENOG41113GY. LUCA.
GeneTreeiENSGT00530000063061.
HOGENOMiHOG000008235.
HOVERGENiHBG096290.
InParanoidiQ7TP36.

Family and domain databases

InterProiIPR014800. ASD1_dom.
IPR014799. ASD2_dom.
IPR027685. Shroom_fam.
[Graphical view]
PANTHERiPTHR15012. PTHR15012. 3 hits.
PfamiPF08688. ASD1. 1 hit.
PF08687. ASD2. 1 hit.
[Graphical view]
PROSITEiPS51306. ASD1. 1 hit.
PS51307. ASD2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7TP36-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPSTVTSRI WWSESSSSSS HDLSGSWEHT SLQRTSDHFS SMGSIDSLDH
60 70 80 90 100
SSQLYPSGHL SSAKSNSSID HLGGHSKRDS AYGSFSTCSS TPDHTLPKAD
110 120 130 140 150
ASSTENILYK VGLWEASRPG SSRQSQSTGD PQGLQDRPSS FLPRVPGNSS
160 170 180 190 200
KSPRPEDNIE PKIATSGRSN FGPVWYVPDK KKAPSPPPLG LPLRSDSFAV
210 220 230 240 250
AARGHEKARG PPFSDLASMQ HFTTLPHVQP RGDRRMETTD RQWKLAHPSS
260 270 280 290 300
GKEIGNVGYQ PEGHLDCRWL CSDDRAGRPS GAPGRHQFSL SSTDVHFLKS
310 320 330 340 350
YHGSQHPQPC SDESPRFPSS PRELLRITPS GCLQEPPELS QDDNPAQVRW
360 370 380 390 400
PGSVNQKLDD RGRSHYFSVP HRQPVHGSAH VLIPRSDYWH SDTTPVDLEC
410 420 430 440 450
PLLRPDQRGY PQQYEETPAS HERGGYQQLN AGIEGCCSGI HEPPRASHTV
460 470 480 490 500
RAGLQCPGND FKLVDAESGR ISRQRTPMLH SLTQDGAWRP GNSKDCGNEK
510 520 530 540 550
PPLLDAQVGK PTRRSDRFAT TLRNEIQMRR AKLQKSKSTV TLAGDSEAED
560 570 580 590 600
CAGDWRVDVG AVPEGSFPST YKEHLKEAQT RVLKATSFQR RDLDPTPADQ
610 620 630 640 650
YPGPPEHRTC DHSASSSLSS FPGEPDSAPR LCEAGLAKPP SSAGGVPHIL
660 670 680 690 700
RIGGRKRFTA EQKLKSYSEP EKINEVGLSG DHSPHPTIRT SEDSVGTFAD
710 720 730 740 750
RWKFFEETSK SLLQKPGHRQ AFCGIPREKA ERPQTQGHEC ESTEPWFQKR
760 770 780 790 800
SRATSCGEIL SEDRKVEKAS EKLNPPRRLG TFAEYQASWK EQKKSLEARS
810 820 830 840 850
SGRYHSADDI LDAGLDQQQR PQYIHERSRS SPSTDHYSQE VPVEPNRQAE
860 870 880 890 900
DSGGQKEALL CTLQAEEGCS APSSSVLSSA QPQDSQHVNE DPTSPQPEAQ
910 920 930 940 950
LSSKCQHLQT STMETSRSPS PQFAPQKLTD KPPLLIHEDN SARYCPVTAC
960 970 980 990 1000
YVFIPCRLQV FVAGALPQLQ TLGIERVMDN NTTVKMVPIK IVHSESQPEK
1010 1020 1030 1040 1050
ESRQSLACPA ELPALPSGLE KDQIKTLSTS EQCYSRFCVY TRQEVETPHR
1060 1070 1080 1090 1100
ARPPEPQPPS TPAPPVRDSC SSPPSLNYGK AKEKTVDDLK SEELAREIVG
1110 1120 1130 1140 1150
KDKSLADILD PSVKIKTTMD LMEGIFPKDE YLLEEAQQRR KLLPKVPSPR
1160 1170 1180 1190 1200
VTEDNSCPSL SAICYNLGTR SKSVPVSQLI KIKILASSPR KQDPGMPGVV
1210 1220 1230 1240 1250
SLATNSTYYS TSAPKAELLI KMKDLQEPEE YSAGDLDHDL SIKKQELIDS
1260 1270 1280 1290 1300
ISRKLQVLRE ARESLLEDIQ ANNALGDEVE AIVKDVCKPN EFDKFRMFIG
1310 1320 1330 1340 1350
DLDKVVNLLL SLSGRLARVE NALNNLDDSP SPGDRQSLLE KQRVLTQQHE
1360 1370 1380 1390 1400
DAKELKENLD RRERIVFDIL ATYLSEENLA DYEHFVKMKS ALIIEQRELE
1410 1420
DKIHLGEEQL KCLFDSLQPE RSK
Length:1,423
Mass (Da):157,989
Last modified:October 1, 2003 - v1
Checksum:i13E5176B51C333C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY325213 mRNA. Translation: AAP92614.1.
UniGeneiRn.16033.

Genome annotation databases

EnsembliENSRNOT00000050819; ENSRNOP00000042259; ENSRNOG00000024322.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY325213 mRNA. Translation: AAP92614.1.
UniGeneiRn.16033.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000056187.

PTM databases

iPTMnetiQ7TP36.
PhosphoSiteiQ7TP36.

Proteomic databases

PaxDbiQ7TP36.
PRIDEiQ7TP36.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000050819; ENSRNOP00000042259; ENSRNOG00000024322.

Organism-specific databases

RGDi1565163. Shroom2.

Phylogenomic databases

eggNOGiENOG410II86. Eukaryota.
ENOG41113GY. LUCA.
GeneTreeiENSGT00530000063061.
HOGENOMiHOG000008235.
HOVERGENiHBG096290.
InParanoidiQ7TP36.

Miscellaneous databases

PROiQ7TP36.

Gene expression databases

ExpressionAtlasiQ7TP36. baseline and differential.

Family and domain databases

InterProiIPR014800. ASD1_dom.
IPR014799. ASD2_dom.
IPR027685. Shroom_fam.
[Graphical view]
PANTHERiPTHR15012. PTHR15012. 3 hits.
PfamiPF08688. ASD1. 1 hit.
PF08687. ASD2. 1 hit.
[Graphical view]
PROSITEiPS51306. ASD1. 1 hit.
PS51307. ASD2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Liver regeneration after PH."
    Xu C.S., Li W.Q., Li Y.C., Yuan J.Y., Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Shi J.B., Rahman S., Wang Q.N., Zhang J.B., Han H.P., Wang G.P., Chai L.Q.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-185; SER-831; SER-918; SER-920 AND SER-1329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSHRM2_RAT
AccessioniPrimary (citable) accession number: Q7TP36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 1, 2003
Last modified: June 8, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.